1kql

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(New page: 200px<br /><applet load="1kql" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kql, resolution 2.70&Aring;" /> '''Crystal structure of...)
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[[Image:1kql.gif|left|200px]]<br /><applet load="1kql" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kql, resolution 2.70&Aring;" />
 
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'''Crystal structure of the C-terminal region of striated muscle alpha-tropomyosin at 2.7 angstrom resolution'''<br />
 
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==Overview==
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==Crystal structure of the C-terminal region of striated muscle alpha-tropomyosin at 2.7 angstrom resolution==
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Contraction in striated and cardiac muscles is regulated by the motions of, a Ca(2+)-sensitive tropomyosin/troponin switch. In contrast, troponin is, absent in other muscle types and in nonmuscle cells, and actomyosin, regulation is myosin-linked. Here we report an unusual crystal structure, at 2.7 A of the C-terminal 31 residues of rat striated-muscle, alpha-tropomyosin (preceded by a fragment of the GCN4 leucine zipper). The, C-terminal 22 residues (263-284) of the structure do not form a, two-stranded alpha-helical coiled coil as does the rest of the molecule, but here the alpha-helices splay apart and are stabilized by the formation, of a tail-to-tail dimer with a symmetry-related molecule. The site of, splaying involves a small group of destabilizing core residues that is, present only in striated muscle tropomyosin isoforms. These results reveal, a specific recognition site for troponin T and clarify the physical basis, for the unique regulatory mechanism of striated muscles.
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<StructureSection load='1kql' size='340' side='right'caption='[[1kql]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1kql]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KQL FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kql OCA], [https://pdbe.org/1kql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kql RCSB], [https://www.ebi.ac.uk/pdbsum/1kql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kql ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TPM1_RAT TPM1_RAT] Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.[https://www.uniprot.org/uniprot/GCN4_YEAST GCN4_YEAST] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kq/1kql_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kql ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1KQL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_and_rattus_norvegicus Saccharomyces cerevisiae and rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KQL OCA].
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*[[Gcn4 3D Structures|Gcn4 3D Structures]]
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*[[Gnc4 3D Structures|Gnc4 3D Structures]]
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==Reference==
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*[[Tropomyosin 3D structures|Tropomyosin 3D structures]]
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The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site., Li Y, Mui S, Brown JH, Strand J, Reshetnikova L, Tobacman LS, Cohen C, Proc Natl Acad Sci U S A. 2002 May 28;99(11):7378-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12032291 12032291]
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__TOC__
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[[Category: Saccharomyces cerevisiae and rattus norvegicus]]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Brown, J.H.]]
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[[Category: Rattus norvegicus]]
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[[Category: Cohen, C.]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Li, Y.]]
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[[Category: Brown JH]]
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[[Category: Mui, S.]]
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[[Category: Cohen C]]
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[[Category: Reshetnikova, L.]]
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[[Category: Li Y]]
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[[Category: Strand, J.]]
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[[Category: Mui S]]
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[[Category: Tobacman, L.S.]]
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[[Category: Reshetnikova L]]
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[[Category: coiled coil]]
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[[Category: Strand J]]
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[[Category: contractile protein]]
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[[Category: Tobacman LS]]
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[[Category: four-helix bundle]]
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[[Category: muscle regulation]]
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[[Category: thin filament]]
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[[Category: tropomyosin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:40:15 2007''
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Current revision

Crystal structure of the C-terminal region of striated muscle alpha-tropomyosin at 2.7 angstrom resolution

PDB ID 1kql

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